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ASSISTANT PROFESSOR MASATOMO SO |
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Osaka University mso@protein.osaka-u.ac.jp |
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SEMINAR | BIOGRAPHY | ||||
Saturday 14th November | Session Five | ||||
Competing pathway of solubility-limited formation of protein aggregates Abstract References [1] Y. Yoshimura, et al (2012) Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation. Proc. Natl. Acad. Sci. USA 109, 14446-14451. [2] M. Adachi, M. So, et al. (2015) Supersaturation-limited and unlimited phase transitions compete to produce the pathway complexity in amyloid fibrillation. J. Biol. Chem. 290, 18134-18145.
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2015-present: Assistant Professor, Institute for Protein Research, Osaka University, Japan Research Fields and Interests: Selected Publications: So, M., Ishii, A., Hata, Y., Yagi, H., Naiki, H., and Goto, Y. (2015) Supersaturation-limited and unlimited phase spaces compete to produce maximal amyloid fibrillation near the critical micelle concentration of sodium dodecyl sulfate. Langmuir, revision submitted. Adachi, M., So, M., Sakurai, K., Kardos, J., and Goto Y. (2015) Supersaturation-limited and unlimited phase transitions compete to produce the pathway complexity in amyloid fibrillation. J. Biol. Chem. 290, 18134-18145. Umemoto, A., Yagi, H., M., So, and Goto Y. (2014) High-throughput analysis of ultrasonication-forced amyloid fibrillation reveals the mechanism underlying the Large Fluctuation in the Lag Time. J. Biol. Chem. 289, 27290-27299. Yoshimura, Y., So, M., Yagi, H., and Goto, Y. (2013) Ultrasonication: an efficient agitation for accelerating the supersaturation-limited amyloid fibrillation of proteins. Jpn. J. Appl. Phys. 52, 07HA01. Yoshimura, Y., Lin, Y., Yagi, H., Lee, Y.-H., Kitayama, H., Sakurai, K., So, M., Ogi, H., Naiki, H., and Goto, Y. (2012) Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation. Proc. Natl. Acad. Sci. USA 109, 14446-14451.
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